2FAU

Crystal structure of human vps26

Summary for 2FAU

• Entry DOI: 10.2210/pdb2fau/pdb
• Descriptor: Vacuolar protein sorting 26, GLYCEROL (3 entities in total)
• Functional Keywords: arrestin, retromer, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O75436
• Total number of polymer chains: 1
• Total formula weight: 40102.70

Authors

Shi, H.,Rojas, R.,Bonifacino, J.S.,Hurley, J.H. (deposition date: 2005-12-08, release date: 2006-05-30, Last modification date: 2024-10-30)

Primary citation

Shi, H.,Rojas, R.,Bonifacino, J.S.,Hurley, J.H.
The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain.
Nat.Struct.Mol.Biol., 13:540-548, 2006

PubMed Abstract: The mammalian retromer complex consists of SNX1, SNX2, Vps26, Vps29 and Vps35, and retrieves lysosomal enzyme receptors from endosomes to the trans-Golgi network. The structure of human Vps26A at 2.1-A resolution reveals two curved beta-sandwich domains connected by a polar core and a flexible linker. Vps26 has an unpredicted structural relationship to arrestins. The Vps35-binding site on Vps26 maps to a mobile loop spanning residues 235-246, near the tip of the C-terminal domain. The loop is phylogenetically conserved and provides a mechanism for Vps26 integration into the complex that leaves the rest of the structure free for engagements with membranes and for conformational changes. Hydrophobic residues and a glycine in this loop are required for integration into the retromer complex and endosomal localization of human Vps26, and for the function of yeast Vps26 in carboxypeptidase Y sorting.

PubMed: 16732284
DOI: 10.1038/nsmb1103

Experimental method

X-RAY DIFFRACTION (2.1 Å)